Year |
Citation |
Score |
2023 |
Brookes E, Rocco M, Vachette P, Trewhella J. AlphaFold-predicted protein structures and small-angle X-ray scattering: insights from an extended examination of selected data in the Small-Angle Scattering Biological Data Bank. Journal of Applied Crystallography. 56: 910-926. PMID 37555230 DOI: 10.1107/S1600576723005344 |
0.342 |
|
2019 |
Berman HM, Adams PD, Bonvin AA, Burley SK, Carragher B, Chiu W, DiMaio F, Ferrin TE, Gabanyi MJ, Goddard TD, Griffin PR, Haas J, Hanke CA, Hoch JC, Hummer G, ... ... Trewhella J, et al. Federating Structural Models and Data: Outcomes from A Workshop on Archiving Integrative Structures. Structure (London, England : 1993). PMID 31780431 DOI: 10.1016/J.Str.2019.11.002 |
0.434 |
|
2019 |
Stokes PH, Robertson NO, Silva AP, Estephan T, Trewhella J, Guss JM, Matthews JM. Mutation in a flexible linker modulates binding affinity for modular complexes. Proteins. PMID 30788856 DOI: 10.1002/Prot.25675 |
0.369 |
|
2019 |
Trewhella J. Reliable Biomolecular Structural Modelling with Small-Angle Scattering Biophysical Journal. 116. DOI: 10.1016/J.Bpj.2018.11.891 |
0.395 |
|
2018 |
Berman HM, Trewhella J, Vallat B, Westbrook JD. Archiving of Integrative Structural Models. Advances in Experimental Medicine and Biology. 1105: 261-272. PMID 30617834 DOI: 10.1007/978-981-13-2200-6_16 |
0.315 |
|
2018 |
Trewhella J. Small Angle Scattering and Structural Biology: Data Quality and Model Validation. Advances in Experimental Medicine and Biology. 1105: 77-100. PMID 30617825 DOI: 10.1007/978-981-13-2200-6_7 |
0.358 |
|
2018 |
Potrzebowski W, Trewhella J, Andre I. Bayesian inference of protein conformational ensembles from limited structural data. Plos Computational Biology. 14: e1006641. PMID 30557358 DOI: 10.1371/Journal.Pcbi.1006641 |
0.391 |
|
2018 |
Gao JL, Kwan AH, Yammine A, Zhou X, Trewhella J, Hugrass BM, Collins DAT, Horne J, Ye P, Harty D, Nguyen KA, Gell DA, Hunter N. Structural properties of a haemophore facilitate targeted elimination of the pathogen Porphyromonas gingivalis. Nature Communications. 9: 4097. PMID 30291238 DOI: 10.2210/Pdb6Crl/Pdb |
0.311 |
|
2018 |
Ryan TM, Trewhella J, Murphy JM, Keown JR, Casey L, Pearce FG, Goldstone DC, Chen K, Luo Z, Kobe B, McDevitt CA, Watkin SA, Hawley AM, Mudie ST, Boban VS, et al. An optimized SEC-SAXS system enabling high X-ray dose for rapid SAXS assessment with correlated UV measurements for biomolecular structure analysis Journal of Applied Crystallography. 51: 97-111. DOI: 10.1107/S1600576717017101 |
0.353 |
|
2017 |
Pozner A, Hudson NO, Trewhella J, Terooatea TW, Miller SA, Buck-Koehntop BA. The C-terminal zinc fingers of ZBTB38 are novel selective readers of DNA methylation. Journal of Molecular Biology. PMID 29287967 DOI: 10.1016/J.Jmb.2017.12.014 |
0.303 |
|
2017 |
Trewhella J, Guss JM. Publication guidelines for biomolecular small-angle scattering: a community-driven effort Acta Crystallographica Section A. 73. DOI: 10.1107/S2053273317081323 |
0.305 |
|
2016 |
Michie KA, Kwan AH, Tung CS, Guss JM, Trewhella J. A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C. Structure (London, England : 1993). PMID 27720588 DOI: 10.1016/J.Str.2016.08.018 |
0.428 |
|
2016 |
Anandapadamanaban M, Pilstål R, Andresen C, Trewhella J, Moche M, Wallner B, Sunnerhagen M. Mutation-Induced Population Shift in the MexR Conformational Ensemble Disengages DNA Binding: A Novel Mechanism for MarR Family Derepression. Structure (London, England : 1993). PMID 27427478 DOI: 10.1016/J.Str.2016.06.008 |
0.33 |
|
2016 |
Trewhella J. Small-angle scattering and 3D structure interpretation. Current Opinion in Structural Biology. 40: 1-7. PMID 27254833 DOI: 10.1016/J.Sbi.2016.05.003 |
0.432 |
|
2016 |
de Diego I, Ksiazek M, Mizgalska D, Koneru L, Golik P, Szmigielski B, Nowak M, Nowakowska Z, Potempa B, Houston JA, Enghild JJ, Thøgersen IB, Gao J, Kwan AH, Trewhella J, et al. The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain. Scientific Reports. 6: 23123. PMID 27005013 DOI: 10.1038/Srep23123 |
0.368 |
|
2015 |
Rubio-Marrero EN, Vincelli G, Jeffries CM, Shaikh TR, Pakos I, Ranaivoson FM, von Daake S, Demeler B, De Jaco A, Perkins G, Ellisman MH, Trewhella J, Comoletti D. Structural characterization of the extracellular domain of CASPR2 and insights into its association with the novel ligand Contactin1. The Journal of Biological Chemistry. PMID 26721881 DOI: 10.1074/Jbc.M115.705681 |
0.407 |
|
2015 |
Nadvi NA, Michie KA, Kwan AH, Guss JM, Trewhella J. Clinically Linked Mutations in the Central Domains of Cardiac Myosin-Binding Protein C with Distinct Phenotypes Show Differential Structural Effects. Structure (London, England : 1993). PMID 26688216 DOI: 10.1016/J.Str.2015.11.001 |
0.385 |
|
2015 |
McGrath AP, Laming EL, Casas Garcia GP, Kvansakul M, Guss JM, Trewhella J, Calmes B, Bernhardt PV, Hanson GR, Kappler U, Maher MJ. Structural basis of interprotein electron transfer in bacterial sulfite oxidation. Elife. 4. PMID 26687009 DOI: 10.7554/Elife.09066 |
0.342 |
|
2015 |
Lee M, Sadowska A, Bekere I, Ho D, Gully BS, Lu Y, Iyer KS, Trewhella J, Fox AH, Bond CS. The structure of human SFPQ reveals a coiled-coil mediated polymer essential for functional aggregation in gene regulation. Nucleic Acids Research. 43: 3826-40. PMID 25765647 DOI: 10.1093/Nar/Gkv156 |
0.375 |
|
2014 |
Millar DP, Trewhella J. Editorial overview--New frontiers of biophysical methods: tools for structural biology and beyond. Current Opinion in Structural Biology. 28: viii-x. PMID 25292464 DOI: 10.1016/J.Sbi.2014.09.005 |
0.301 |
|
2013 |
Trewhella J, Hendrickson WA, Kleywegt GJ, Sali A, Sato M, Schwede T, Svergun DI, Tainer JA, Westbrook J, Berman HM. Report of the wwPDB Small-Angle Scattering Task Force: data requirements for biomolecular modeling and the PDB. Structure (London, England : 1993). 21: 875-81. PMID 23747111 DOI: 10.1016/J.Str.2013.04.020 |
0.356 |
|
2012 |
Taylor JE, Chow JY, Jeffries CM, Kwan AH, Duff AP, Hamilton WA, Trewhella J. Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release. Biophysical Journal. 103: 541-9. PMID 22947870 DOI: 10.1016/J.Bpj.2012.06.042 |
0.38 |
|
2012 |
Bhati M, Lee C, Gadd MS, Jeffries CM, Kwan A, Whitten AE, Trewhella J, Mackay JP, Matthews JM. Solution structure of the LIM-homeodomain transcription factor complex Lhx3/Ldb1 and the effects of a pituitary mutation on key Lhx3 interactions. Plos One. 7: e40719. PMID 22848397 DOI: 10.1371/Journal.Pone.0040719 |
0.389 |
|
2012 |
Lu Y, Kwan AH, Jeffries CM, Guss JM, Trewhella J. The motif of human cardiac myosin-binding protein C is required for its Ca2+-dependent interaction with calmodulin. The Journal of Biological Chemistry. 287: 31596-607. PMID 22801425 DOI: 10.1074/Jbc.M112.383299 |
0.358 |
|
2012 |
Jacques DA, Guss JM, Svergun DI, Trewhella J. Publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution. Acta Crystallographica. Section D, Biological Crystallography. 68: 620-6. PMID 22683784 DOI: 10.1107/S0907444912012073 |
0.384 |
|
2012 |
Jacques DA, Guss JM, Trewhella J. Reliable structural interpretation of small-angle scattering data from bio-molecules in solution--the importance of quality control and a standard reporting framework. Bmc Structural Biology. 12: 9. PMID 22595034 DOI: 10.1186/1472-6807-12-9 |
0.407 |
|
2012 |
Hynson RM, Jeffries CM, Trewhella J, Cocklin S. Solution structure studies of monomeric human TIP47/perilipin-3 reveal a highly extended conformation. Proteins. 80: 2046-55. PMID 22508559 DOI: 10.1002/Prot.24095 |
0.409 |
|
2012 |
Seckler JM, Trewhella J, Barkley MD, Wintrode PL. HIV-1 Reverse Transcriptase Monomers Adopt Multiple Conformations in Solution Biophysical Journal. 102: 46a-47a. DOI: 10.1016/J.Bpj.2011.11.284 |
0.371 |
|
2011 |
Taraban MB, Ramachandran S, Gryczynski I, Gryczynski Z, Trewhella J, Yu YB. Effects of chain length on oligopeptide hydrogelation. Soft Matter. 7: 2624-2631. PMID 22287980 DOI: 10.1039/C0Sm00919A |
0.311 |
|
2011 |
Jeffries CM, Lu Y, Hynson RM, Taylor JE, Ballesteros M, Kwan AH, Trewhella J. Human cardiac myosin binding protein C: structural flexibility within an extended modular architecture. Journal of Molecular Biology. 414: 735-48. PMID 22041450 DOI: 10.1016/J.Jmb.2011.10.029 |
0.392 |
|
2011 |
Gadd MS, Bhati M, Jeffries CM, Langley DB, Trewhella J, Guss JM, Matthews JM. Structural basis for partial redundancy in a class of transcription factors, the LIM homeodomain proteins, in neural cell type specification. The Journal of Biological Chemistry. 286: 42971-80. PMID 22025611 DOI: 10.1074/Jbc.M111.248559 |
0.388 |
|
2011 |
Lu Y, Kwan AH, Trewhella J, Jeffries CM. The C0C1 fragment of human cardiac myosin binding protein C has common binding determinants for both actin and myosin. Journal of Molecular Biology. 413: 908-13. PMID 21978665 DOI: 10.1016/J.Jmb.2011.09.026 |
0.378 |
|
2011 |
Johansen D, Trewhella J, Goldenberg DP. Fractal dimension of an intrinsically disordered protein: small-angle X-ray scattering and computational study of the bacteriophage λ N protein. Protein Science : a Publication of the Protein Society. 20: 1955-70. PMID 21936008 DOI: 10.1002/Pro.739 |
0.405 |
|
2011 |
Orlova A, Galkin VE, Jeffries CM, Egelman EH, Trewhella J. The N-terminal domains of myosin binding protein C can bind polymorphically to F-actin. Journal of Molecular Biology. 412: 379-86. PMID 21821050 DOI: 10.1016/J.Jmb.2011.07.056 |
0.35 |
|
2011 |
Zhai Q, Landesman MB, Chung HY, Dierkers A, Jeffries CM, Trewhella J, Hill CP, Sundquist WI. Activation of the retroviral budding factor ALIX. Journal of Virology. 85: 9222-6. PMID 21715492 DOI: 10.1128/Jvi.02653-10 |
0.304 |
|
2011 |
Lu Y, Jeffries CM, Trewhella J. Invited review: probing the structures of muscle regulatory proteins using small-angle solution scattering. Biopolymers. 95: 505-16. PMID 21442605 DOI: 10.1002/Bip.21624 |
0.441 |
|
2011 |
Johansen D, Jeffries CM, Hammouda B, Trewhella J, Goldenberg DP. Effects of macromolecular crowding on an intrinsically disordered protein characterized by small-angle neutron scattering with contrast matching. Biophysical Journal. 100: 1120-8. PMID 21320458 DOI: 10.1016/J.Bpj.2011.01.020 |
0.396 |
|
2011 |
Jacques DA, Langley DB, Kuramitsu S, Yokoyama S, Trewhella J, Guss JM. The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase. Acta Crystallographica. Section D, Biological Crystallography. 67: 105-11. PMID 21245531 DOI: 10.1107/S0907444910051127 |
0.349 |
|
2011 |
Jacques DA, Langley DB, Hynson RM, Whitten AE, Kwan A, Guss JM, Trewhella J. A novel structure of an antikinase and its inhibitor. Journal of Molecular Biology. 405: 214-26. PMID 21050859 DOI: 10.1016/J.Jmb.2010.10.047 |
0.402 |
|
2011 |
Chow JYH, Jeffries CM, Kwan AH, Guss JM, Trewhella J. Corrigendum to “Calmodulin Disrupts the Structure of the HIV-1 MA Protein” [J. Mol. Biol. 400/4 (2010) 702–714] Journal of Molecular Biology. 413: 742. DOI: 10.1016/J.Jmb.2011.09.003 |
0.304 |
|
2010 |
Fenton AW, Williams R, Trewhella J. Changes in small-angle X-ray scattering parameters observed upon binding of ligand to rabbit muscle pyruvate kinase are not correlated with allosteric transitions. Biochemistry. 49: 7202-9. PMID 20712377 DOI: 10.1021/Bi100147W |
0.393 |
|
2010 |
Siddiqui KS, Poljak A, De Francisci D, Guerriero G, Pilak O, Burg D, Raftery MJ, Parkin DM, Trewhella J, Cavicchioli R. A chemically modified alpha-amylase with a molten-globule state has entropically driven enhanced thermal stability. Protein Engineering, Design & Selection : Peds. 23: 769-80. PMID 20696745 DOI: 10.1093/Protein/Gzq051 |
0.321 |
|
2010 |
Comoletti D, Miller MT, Jeffries CM, Wilson J, Demeler B, Taylor P, Trewhella J, Nakagawa T. The macromolecular architecture of extracellular domain of alphaNRXN1: domain organization, flexibility, and insights into trans-synaptic disposition. Structure (London, England : 1993). 18: 1044-53. PMID 20696403 DOI: 10.1016/J.Str.2010.06.005 |
0.389 |
|
2010 |
Hynson RM, Kwan AH, Jacques DA, Mackay JP, Trewhella J. 1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis. Biomolecular Nmr Assignments. 4: 167-9. PMID 20524093 DOI: 10.1007/S12104-010-9237-6 |
0.315 |
|
2010 |
Chow JY, Jeffries CM, Kwan AH, Guss JM, Trewhella J. Calmodulin disrupts the structure of the HIV-1 MA protein. Journal of Molecular Biology. 400: 702-14. PMID 20488189 DOI: 10.1016/J.Jmb.2010.05.022 |
0.426 |
|
2010 |
Ramachandran S, Taraban MB, Trewhella J, Gryczynski I, Gryczynski Z, Yu YB. Effect of temperature during assembly on the structure and mechanical properties of peptide-based materials. Biomacromolecules. 11: 1502-6. PMID 20481580 DOI: 10.1021/Bm100138M |
0.324 |
|
2010 |
Cross AJ, Jeffries CM, Trewhella J, Matthews JM. LIM domain binding proteins 1 and 2 have different oligomeric states. Journal of Molecular Biology. 399: 133-44. PMID 20382157 DOI: 10.1016/J.Jmb.2010.04.006 |
0.389 |
|
2010 |
Jacques DA, Trewhella J. Small-angle scattering for structural biology--expanding the frontier while avoiding the pitfalls. Protein Science : a Publication of the Protein Society. 19: 642-57. PMID 20120026 DOI: 10.1002/Pro.351 |
0.425 |
|
2010 |
Orlova A, Galkin VE, Jeffries CM, Trewhella J, Egelman EH. Binding of N-Terminus Fragments of Cardiac Myosin-Binding C-protein to Actin Biophysical Journal. 98: 157a. DOI: 10.1016/J.Bpj.2009.12.845 |
0.355 |
|
2009 |
Whitten AE, Smith BJ, Menting JG, Margetts MB, McKern NM, Lovrecz GO, Adams TE, Richards K, Bentley JD, Trewhella J, Ward CW, Lawrence MC. Solution structure of ectodomains of the insulin receptor family: the ectodomain of the type 1 insulin-like growth factor receptor displays asymmetry of ligand binding accompanied by limited conformational change. Journal of Molecular Biology. 394: 878-92. PMID 19835884 DOI: 10.1016/J.Jmb.2009.10.011 |
0.327 |
|
2009 |
Whitten AE, Trewhella J. Small-angle scattering and neutron contrast variation for studying bio-molecular complexes. Methods in Molecular Biology (Clifton, N.J.). 544: 307-23. PMID 19488708 DOI: 10.1007/978-1-59745-483-4_20 |
0.45 |
|
2009 |
Jacques DA, Streamer M, Rowland SL, King GF, Guss JM, Trewhella J, Langley DB. Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state. Acta Crystallographica. Section D, Biological Crystallography. 65: 574-81. PMID 19465772 DOI: 10.1107/S090744490901169X |
0.396 |
|
2009 |
Mills RD, Trewhella J, Qiu TW, Welte T, Ryan TM, Hanley T, Knott RB, Lithgow T, Mulhern TD. Domain organization of the monomeric form of the Tom70 mitochondrial import receptor. Journal of Molecular Biology. 388: 1043-58. PMID 19358854 DOI: 10.1016/J.Jmb.2009.03.070 |
0.405 |
|
2009 |
Siddiqui KS, Parkin DM, Curmi PM, De Francisci D, Poljak A, Barrow K, Noble MH, Trewhella J, Cavicchioli R. A novel approach for enhancing the catalytic efficiency of a protease at low temperature: reduction in substrate inhibition by chemical modification. Biotechnology and Bioengineering. 103: 676-86. PMID 19288442 DOI: 10.1002/Bit.22300 |
0.31 |
|
2009 |
Claridge JK, Headey SJ, Chow JY, Schwalbe M, Edwards PJ, Jeffries CM, Venugopal H, Trewhella J, Pascal SM. A picornaviral loop-to-loop replication complex. Journal of Structural Biology. 166: 251-62. PMID 19268541 DOI: 10.1016/J.Jsb.2009.02.010 |
0.418 |
|
2008 |
Whitten AE, Jeffries CM, Harris SP, Trewhella J. Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function. Proceedings of the National Academy of Sciences of the United States of America. 105: 18360-5. PMID 19011110 DOI: 10.1073/Pnas.0808903105 |
0.35 |
|
2008 |
Jacques DA, Langley DB, Jeffries CM, Cunningham KA, Burkholder WF, Guss JM, Trewhella J. Histidine kinase regulation by a cyclophilin-like inhibitor. Journal of Molecular Biology. 384: 422-35. PMID 18823995 DOI: 10.1016/J.Jmb.2008.09.017 |
0.373 |
|
2008 |
Zhan H, Taraban M, Trewhella J, Swint-Kruse L. Subdividing repressor function: DNA binding affinity, selectivity, and allostery can be altered by amino acid substitution of nonconserved residues in a LacI/GalR homologue. Biochemistry. 47: 8058-69. PMID 18616293 DOI: 10.1021/Bi800443K |
0.347 |
|
2008 |
Griffin MD, Dobson RC, Pearce FG, Antonio L, Whitten AE, Liew CK, Mackay JP, Trewhella J, Jameson GB, Perugini MA, Gerrard JA. Evolution of quaternary structure in a homotetrameric enzyme. Journal of Molecular Biology. 380: 691-703. PMID 18556019 DOI: 10.1016/J.Jmb.2008.05.038 |
0.359 |
|
2008 |
Comoletti D, Grishaev A, Whitten AE, Taylor P, Trewhella J. Characterization of the solution structure of a neuroligin/beta-neurexin complex. Chemico-Biological Interactions. 175: 150-5. PMID 18550038 DOI: 10.1016/J.Cbi.2008.04.040 |
0.403 |
|
2008 |
Trewhella J. The different views from small angles. Proceedings of the National Academy of Sciences of the United States of America. 105: 4967-8. PMID 18362330 DOI: 10.1073/Pnas.0801324105 |
0.401 |
|
2008 |
Wang Y, Trewhella J, Goldenberg DP. Small-angle X-ray scattering of reduced ribonuclease A: effects of solution conditions and comparisons with a computational model of unfolded proteins. Journal of Molecular Biology. 377: 1576-92. PMID 18329044 DOI: 10.1016/J.Jmb.2008.02.009 |
0.41 |
|
2008 |
Jeffries CM, Whitten AE, Harris SP, Trewhella J. Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C. Journal of Molecular Biology. 377: 1186-99. PMID 18313073 DOI: 10.1016/J.Jmb.2008.01.080 |
0.394 |
|
2008 |
Taraban M, Zhan H, Whitten AE, Langley DB, Matthews KS, Swint-Kruse L, Trewhella J. Ligand-induced conformational changes and conformational dynamics in the solution structure of the lactose repressor protein. Journal of Molecular Biology. 376: 466-81. PMID 18164724 DOI: 10.1016/J.Jmb.2007.11.067 |
0.442 |
|
2008 |
Grishaev A, Tugarinov V, Kay LE, Trewhella J, Bax A. Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. Journal of Biomolecular Nmr. 40: 95-106. PMID 18008171 DOI: 10.1007/S10858-007-9211-5 |
0.44 |
|
2008 |
Chow JYH, Claridge JK, Jeffries C, Headley SJ, Soares GA, Schwalbe M, Pascal SM, Trewhella J. The interaction between human rhinovirus 3C protease and stem loop D studied by solution scattering Acta Crystallographica Section A. 64: 214-214. DOI: 10.1107/S0108767308093136 |
0.317 |
|
2008 |
Jeffries C, Whitten A, Harris S, Trewhella J. Small-angle scattering: the regulatory domains of cardiac C-protein and their complex with F-actin Acta Crystallographica Section a Foundations of Crystallography. 64: C297-C297. DOI: 10.1107/S010876730809051X |
0.382 |
|
2008 |
Whitten A, Jeffries C, Harris S, Trewhella J. A small-angle neutron contrast variation study of the complex of actin and myosin binding protein C Acta Crystallographica Section a Foundations of Crystallography. 64: C297-C297. DOI: 10.1107/S0108767308090508 |
0.409 |
|
2008 |
Whitten AE, Cai S, Trewhella J. MULCh: Modules for the analysis of small-angle neutron contrast variation data from biomolecular assemblies Journal of Applied Crystallography. 41: 222-226. DOI: 10.1107/S0021889807055136 |
0.37 |
|
2007 |
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M. Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. Journal of Molecular Biology. 373: 1269-80. PMID 17915250 DOI: 10.1016/J.Jmb.2007.08.057 |
0.361 |
|
2007 |
Howarth JW, Meller J, Solaro RJ, Trewhella J, Rosevear PR. Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin. Journal of Molecular Biology. 373: 706-22. PMID 17854829 DOI: 10.1016/J.Jmb.2007.08.035 |
0.368 |
|
2007 |
Comoletti D, Grishaev A, Whitten AE, Tsigelny I, Taylor P, Trewhella J. Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering. Structure (London, England : 1993). 15: 693-705. PMID 17562316 DOI: 10.1016/J.Str.2007.04.010 |
0.453 |
|
2007 |
Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, Guss JM, Trewhella J, Langley DB. The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. Journal of Molecular Biology. 368: 407-20. PMID 17350039 DOI: 10.1016/J.Jmb.2007.01.064 |
0.415 |
|
2006 |
Trewhella J. Structural themes and variations in protein kinase A as seen by small-angle scattering and neutron contrast variation. European Biophysics Journal : Ebj. 35: 585-9. PMID 16625363 DOI: 10.1007/S00249-006-0061-Y |
0.444 |
|
2006 |
Trewhella J. Protein kinase A targeting and activation as seen by small-angle solution scattering. European Journal of Cell Biology. 85: 655-62. PMID 16460833 DOI: 10.1016/J.Ejcb.2006.01.003 |
0.46 |
|
2006 |
Vigil D, Blumenthal DK, Taylor SS, Trewhella J. Solution scattering reveals large differences in the global structures of type II protein kinase A isoforms. Journal of Molecular Biology. 357: 880-9. PMID 16460759 DOI: 10.1016/J.Jmb.2006.01.006 |
0.448 |
|
2006 |
Ramachandran S, Trewhella J, Tseng Y, Yu YB. Coassembling peptide-based biomaterials: Effects of pairing equal and unequal chain length oligopeptides Chemistry of Materials. 18: 6157-6162. DOI: 10.1021/Cm061071L |
0.316 |
|
2006 |
Trewhella J. Neutrons reveal how nature uses structural themes and variation in biological regulation Physica B: Condensed Matter. 385: 825-830. DOI: 10.1016/J.Physb.2006.05.118 |
0.403 |
|
2005 |
Grishaev A, Wu J, Trewhella J, Bax A. Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data. Journal of the American Chemical Society. 127: 16621-8. PMID 16305251 DOI: 10.1021/Ja054342M |
0.451 |
|
2005 |
Priddy TS, MacDonald BA, Heller WT, Nadeau OW, Trewhella J, Carlson GM. Ca2+-induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering. Protein Science : a Publication of the Protein Society. 14: 1039-48. PMID 15741333 DOI: 10.1110/Ps.041124705 |
0.395 |
|
2004 |
Vigil D, Blumenthal DK, Brown S, Taylor SS, Trewhella J. Differential effects of substrate on type I and type II PKA holoenzyme dissociation. Biochemistry. 43: 5629-36. PMID 15134437 DOI: 10.1021/Bi0499157 |
0.332 |
|
2004 |
Vigil D, Blumenthal DK, Heller WT, Brown S, Canaves JM, Taylor SS, Trewhella J. Conformational differences among solution structures of the type Ialpha, IIalpha and IIbeta protein kinase A regulatory subunit homodimers: role of the linker regions. Journal of Molecular Biology. 337: 1183-94. PMID 15046986 DOI: 10.1016/J.Jmb.2004.02.028 |
0.4 |
|
2004 |
Heller WT, Vigil D, Brown S, Blumenthal DK, Taylor SS, Trewhella J. C subunits binding to the protein kinase A RI alpha dimer induce a large conformational change. The Journal of Biological Chemistry. 279: 19084-90. PMID 14985329 DOI: 10.1074/Jbc.M313405200 |
0.378 |
|
2003 |
Heller WT, Krueger JK, Trewhella J. Further insights into calmodulin-myosin light chain kinase interaction from solution scattering and shape restoration. Biochemistry. 42: 10579-88. PMID 12962481 DOI: 10.1021/Bi0348664 |
0.4 |
|
2003 |
Heller WT, Finley NL, Dong WJ, Timmins P, Cheung HC, Rosevear PR, Trewhella J. Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation. Biochemistry. 42: 7790-800. PMID 12820888 DOI: 10.1021/Bi0341509 |
0.422 |
|
2003 |
Wall ME, Francis SH, Corbin JD, Grimes K, Richie-Jannetta R, Kotera J, Macdonald BA, Gibson RR, Trewhella J. Mechanisms associated with cGMP binding and activation of cGMP-dependent protein kinase. Proceedings of the National Academy of Sciences of the United States of America. 100: 2380-5. PMID 12591946 DOI: 10.1073/Pnas.0534892100 |
0.654 |
|
2003 |
Harris SP, Heller WT, Greaser ML, Moss RL, Trewhella J. Solution structure of heavy meromyosin by small-angle scattering. The Journal of Biological Chemistry. 278: 6034-40. PMID 12466269 DOI: 10.1074/Jbc.M210558200 |
0.421 |
|
2002 |
Heller WT, Abusamhadneh E, Finley N, Rosevear PR, Trewhella J. The solution structure of a cardiac troponin C-troponin I-troponin T complex shows a somewhat compact troponin C interacting with an extended troponin I-troponin T component. Biochemistry. 41: 15654-63. PMID 12501194 DOI: 10.1021/Bi026687C |
0.412 |
|
2002 |
Trewhella J, Krueger JK. Small-angle solution scattering reveals information on conformational dynamics in calcium-binding proteins and in their interactions with regulatory targets. Methods in Molecular Biology (Clifton, N.J.). 173: 137-59. PMID 11859757 DOI: 10.1385/1-59259-184-1:137 |
0.387 |
|
2002 |
Tung CS, Walsh DA, Trewhella J. A structural model of the catalytic subunit-regulatory subunit dimeric complex of the cAMP-dependent protein kinase. The Journal of Biological Chemistry. 277: 12423-31. PMID 11799117 DOI: 10.1074/Jbc.M110298200 |
0.37 |
|
2001 |
Vigil D, Gallagher SC, Trewhella J, GarcÃa AE. Functional dynamics of the hydrophobic cleft in the N-domain of calmodulin. Biophysical Journal. 80: 2082-92. PMID 11325712 DOI: 10.1016/S0006-3495(01)76182-6 |
0.416 |
|
2001 |
Krueger JK, Gallagher SC, Zhi G, Geguchadze R, Persechini A, Stull JT, Trewhella J. Activation of myosin light chain kinase requires translocation of bound calmodulin. The Journal of Biological Chemistry. 276: 4535-8. PMID 11124250 DOI: 10.1074/Jbc.C000857200 |
0.422 |
|
2000 |
Wall ME, Gallagher SC, Trewhella J. Large-scale shape changes in proteins and macromolecular complexes. Annual Review of Physical Chemistry. 51: 355-80. PMID 11031286 DOI: 10.1146/Annurev.Physchem.51.1.355 |
0.647 |
|
2000 |
Tung CS, Wall ME, Gallagher SC, Trewhella J. A model of troponin-I in complex with troponin-C using hybrid experimental data: the inhibitory region is a beta-hairpin. Protein Science : a Publication of the Protein Society. 9: 1312-26. PMID 10933496 DOI: 10.1110/Ps.9.7.1312 |
0.672 |
|
2000 |
Krueger JK, Gallagher SC, Wang CA, Trewhella J. Calmodulin remains extended upon binding to smooth muscle caldesmon: a combined small-angle scattering and fourier transform infrared spectroscopy study. Biochemistry. 39: 3979-87. PMID 10747786 DOI: 10.1021/Bi992638X |
0.435 |
|
1999 |
Krueger JK, McCrary BS, Wang AH, Shriver JW, Trewhella J, Edmondson SP. The solution structure of the Sac7d/DNA complex: a small-angle X-ray scattering study. Biochemistry. 38: 10247-55. PMID 10441118 DOI: 10.1021/Bi990782C |
0.418 |
|
1999 |
Hernández G, Blumenthal DK, Kennedy MA, Unkefer CJ, Trewhella J. Troponin I inhibitory peptide (96-115) has an extended conformation when bound to skeletal muscle troponin C. Biochemistry. 38: 6911-7. PMID 10346913 DOI: 10.1021/Bi990150Q |
0.322 |
|
1999 |
Gallagher SC, Callaghan AJ, Zhao J, Dalton H, Trewhella J. Global conformational changes control the reactivity of methane monooxygenase. Biochemistry. 38: 6752-60. PMID 10346895 DOI: 10.1021/Bi982991N |
0.414 |
|
1999 |
Zhao J, Wang J, Chen DJ, Peterson SR, Trewhella J. The solution structure of the DNA double-stranded break repair protein Ku and its complex with DNA: a neutron contrast variation study. Biochemistry. 38: 2152-9. PMID 10026299 DOI: 10.1021/Bi9825246 |
0.314 |
|
1998 |
Krueger JK, Bishop NA, Blumenthal DK, Zhi G, Beckingham K, Stull JT, Trewhella J. Calmodulin binding to myosin light chain kinase begins at substoichiometric Ca2+ concentrations: a small-angle scattering study of binding and conformational transitions. Biochemistry. 37: 17810-7. PMID 9922147 DOI: 10.1021/Bi981656W |
0.353 |
|
1998 |
Stull JT, Lin PJ, Krueger JK, Trewhella J, Zhi G. Myosin light chain kinase: functional domains and structural motifs. Acta Physiologica Scandinavica. 164: 471-82. PMID 9887970 DOI: 10.1111/J.1365-201X.1998.Tb10699.X |
0.338 |
|
1998 |
Improta S, Krueger JK, Gautel M, Atkinson RA, Lefèvre JF, Moulton S, Trewhella J, Pastore A. The assembly of immunoglobulin-like modules in titin: implications for muscle elasticity. Journal of Molecular Biology. 284: 761-77. PMID 9826514 DOI: 10.1006/Jmbi.1998.2028 |
0.386 |
|
1998 |
Zhao J, Hoye E, Boylan S, Walsh DA, Trewhella J. Quaternary structures of a catalytic subunit-regulatory subunit dimeric complex and the holoenzyme of the cAMP-dependent protein kinase by neutron contrast variation. The Journal of Biological Chemistry. 273: 30448-59. PMID 9804812 DOI: 10.1074/Jbc.273.46.30448 |
0.402 |
|
1998 |
Krueger JK, Zhi G, Stull JT, Trewhella J. Neutron-scattering studies reveal further details of the Ca2+/calmodulin-dependent activation mechanism of myosin light chain kinase. Biochemistry. 37: 13997-4004. PMID 9760234 DOI: 10.1021/Bi981311D |
0.419 |
|
1998 |
Trewhella J, Gallagher SC, Krueger JK, Zhao J. Neutron and X-ray solution scattering provide insights into biomolecular structure and function. Science Progress. 81: 101-22. PMID 9717472 |
0.316 |
|
1997 |
Zhao J, Trewhella J, Corbin J, Francis S, Mitchell R, Brushia R, Walsh D. Progressive cyclic nucleotide-induced conformational changes in the cGMP-dependent protein kinase studied by small angle X-ray scattering in solution. The Journal of Biological Chemistry. 272: 31929-36. PMID 9395542 DOI: 10.1074/Jbc.272.50.31929 |
0.435 |
|
1997 |
Trewhella J. Insights into biomolecular function from small-angle scattering. Current Opinion in Structural Biology. 7: 702-8. PMID 9345630 DOI: 10.1016/S0959-440X(97)80081-4 |
0.385 |
|
1997 |
Krueger JK, Olah GA, Rokop SE, Zhi G, Stull JT, Trewhella J. Structures of calmodulin and a functional myosin light chain kinase in the activated complex: a neutron scattering study. Biochemistry. 36: 6017-23. PMID 9166772 DOI: 10.1021/Bi9702703 |
0.424 |
|
1997 |
Seeger PA, Rokop SE, Palmer PD, Henderson SJ, Hobart DE, Trewhella J. Neutron resonance scattering shows specific binding of plutonium to the calcium-binding sites of the protein calmodulin and yields precise distance information Journal of the American Chemical Society. 119: 5118-5125. DOI: 10.1021/Ja9633124 |
0.429 |
|
1996 |
Olah GA, Trewhella J. The structure of the muscle protein complex 4Ca2+.troponin C.troponin I. Monte Carlo modeling analysis of small-angle X-ray data. Basic Life Sciences. 64: 137-47. PMID 9031509 |
0.316 |
|
1996 |
Sunnerhagen M, Olah GA, Stenflo J, Forsén S, Drakenberg T, Trewhella J. The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study. Biochemistry. 35: 11547-59. PMID 8794734 DOI: 10.1021/Bi960633J |
0.365 |
|
1995 |
Glass DB, Trewhella J, Mitchell RD, Walsh DA. Conformationally constrained analogs of protein kinase inhibitor (6-22)amide: effect of turn structures in the center of the peptide on inhibition of cAMP-dependent protein kinase. Protein Science : a Publication of the Protein Society. 4: 405-15. PMID 7795524 DOI: 10.1002/Pro.5560040307 |
0.389 |
|
1995 |
Olah GA, Gray DM, Gray CW, Kergil DL, Sosnick TR, Mark BL, Vaughan MR, Trewhella J. Structures of fd gene 5 protein.nucleic acid complexes: a combined solution scattering and electron microscopy study. Journal of Molecular Biology. 249: 576-94. PMID 7783213 DOI: 10.1006/Jmbi.1995.0320 |
0.616 |
|
1994 |
Olah GA, Rokop SE, Wang CL, Blechner SL, Trewhella J. Troponin I encompasses an extended troponin C in the Ca(2+)-bound complex: a small-angle X-ray and neutron scattering study. Biochemistry. 33: 8233-9. PMID 8031757 DOI: 10.1021/Bi00193A009 |
0.397 |
|
1994 |
Olah GA, Trewhella J. A model structure of the muscle protein complex 4Ca2+.troponin C.troponin I derived from small-angle scattering data: implications for regulation. Biochemistry. 33: 12800-6. PMID 7947685 DOI: 10.1021/Bi00209A011 |
0.417 |
|
1993 |
Olah GA, Mitchell RD, Sosnick TR, Walsh DA, Trewhella J. Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptide. Biochemistry. 32: 3649-57. PMID 8385485 DOI: 10.1021/Bi00065A018 |
0.633 |
|
1992 |
Sosnick TR, Benjamin DC, Novotny J, Seeger PA, Trewhella J. Distances between the antigen-binding sites of three murine antibody subclasses measured using neutron and X-ray scattering. Biochemistry. 31: 1779-86. PMID 1737031 DOI: 10.1021/Bi00121A028 |
0.588 |
|
1992 |
Henderson SJ, Newsholme P, Heidorn DB, Mitchell R, Seeger PA, Walsh DA, Trewhella J. Solution structure of phosphorylase kinase studied using small-angle X-ray and neutron scattering. Biochemistry. 31: 437-42. PMID 1731902 DOI: 10.1021/Bi00117A019 |
0.423 |
|
1992 |
Sosnick TR, Trewhella J. Denatured states of ribonuclease A have compact dimensions and residual secondary structure. Biochemistry. 31: 8329-35. PMID 1525171 |
0.543 |
|
1992 |
Trewhella J. The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains. Cell Calcium. 13: 377-90. PMID 1505003 DOI: 10.1016/0143-4160(92)90051-S |
0.46 |
|
1992 |
Blechner SL, Olah GA, Strynadka NC, Hodges RS, Trewhella J. 4Ca2+.troponin C forms dimers in solution at neutral pH that dissociate upon binding various peptides: small-angle X-ray scattering studies of peptide-induced structural changes. Biochemistry. 31: 11326-34. PMID 1445871 DOI: 10.1021/Bi00161A010 |
0.401 |
|
1992 |
Cranberg L, Trewhella J, Glyde HR. Naysaying the Neutron Scattering Society Physics Today. 45: 15. DOI: 10.1063/1.2809905 |
0.337 |
|
1991 |
Sosnick T, Charles S, Stubbs G, Yau P, Bradbury EM, Timmins P, Trewhella J. Orienting rigid and flexible biological assemblies in ferrofluids for small-angle neutron scattering studies. Biophysical Journal. 60: 1178-89. PMID 19431809 DOI: 10.1016/S0006-3495(91)82153-1 |
0.727 |
|
1990 |
Trewhella J, Blumenthal DK, Rokop SE, Seeger PA. Small-angle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase Biochemistry®. 29: 9316-9324. PMID 2248948 DOI: 10.1021/Bi00492A003 |
0.424 |
|
1990 |
Seeger PA, Williams A, Trewhella J. The Low-Q Diffractometer at the Los Alamos Neutron Scattering Center Molecular Crystals and Liquid Crystals. 180: 101-117. DOI: 10.1080/00268949008025793 |
0.319 |
|
1990 |
Trewhella J, Heidorn DB, Seeger PA. Solution structures of calcium regulating proteins: A small-angle scattering study Molecular Crystals and Liquid Crystals. 180: 45-53. DOI: 10.1080/00268949008025787 |
0.435 |
|
1989 |
Heidorn DB, Seeger PA, Rokop SE, Blumenthal DK, Means AR, Crespi H, Trewhella J. Changes in the structure of calmodulin induced by a peptide based on the calmodulin-binding domain of myosin light chain kinase. Biochemistry. 28: 6757-64. PMID 2790029 DOI: 10.1021/Bi00442A032 |
0.414 |
|
1989 |
Trewhella J, Kevin Liddle W, Heidorn DB, Strynadka N. Calmodulin and troponin C structures studied by Fourier transform infrared spectroscopy: Effects of Ca2+ and Mg2+ binding Biochemistry. 28: 1294-1301. PMID 2713365 DOI: 10.1021/Bi00429A052 |
0.341 |
|
1989 |
Reed J, De Ropp JS, Trewhella J, Glass DB, Liddle WK, Bradbury EM, Kinzel V, Walsh DA. Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase. The Biochemical Journal. 264: 371-80. PMID 2604724 DOI: 10.1042/Bj2640371 |
0.397 |
|
1989 |
Kowluru RA, Heidorn DB, Edmondson SP, Bitensky MW, Kowluru A, Downer NW, Whaley TW, Trewhella J. Glycation of calmodulin: Chemistry and structural and functional consequences Biochemistry. 28: 2220-2228. PMID 2541779 DOI: 10.1021/Bi00431A038 |
0.326 |
|
1989 |
Hayter JB, Pynn R, Charles S, Skjeltorp AT, Trewhella J, Stubbs G, Timmins P. Ordered macromolecular structures in ferrofluid mixtures Physical Review Letters. 62: 1667-1670. DOI: 10.1103/Physrevlett.62.1667 |
0.317 |
|
1988 |
Heidorn DB, Trewhella J. Comparison of the crystal and solution structures of calmodulin and troponin C Biochemistry. 27: 909-915. PMID 3365370 DOI: 10.1021/Bi00403A011 |
0.385 |
|
1988 |
Trewhella J, Carlson VA, Curtis EH, Heidorn DB. Differences in the solution structures of oxidized and reduced cytochrome c measured by small-angle X-ray scattering. Biochemistry. 27: 1121-5. PMID 2835084 DOI: 10.1021/Bi00404A007 |
0.395 |
|
1986 |
Trewhella J, Popot JL, Zaccaï G, Engelman DM. Localization of two chymotryptic fragments in the structure of renatured bacteriorhodopsin by neutron diffraction. The Embo Journal. 5: 3045-9. PMID 3792306 DOI: 10.1002/J.1460-2075.1986.Tb04604.X |
0.573 |
|
1986 |
Popot JL, Trewhella J, Engelman DM. Reformation of crystalline purple membrane from purified bacteriorhodopsin fragments. The Embo Journal. 5: 3039-44. PMID 3792305 DOI: 10.1002/J.1460-2075.1986.Tb04603.X |
0.533 |
|
1986 |
Trewhella J, Eckert J. Inelastic neutron scattering in biology Physica B+C. 136: 507-511. DOI: 10.1016/S0378-4363(86)80129-2 |
0.351 |
|
1986 |
Cusack S, Smith J, Finney J, Karplus M, Trewhella J. Low frequency dynamics of proteins studied by neutron time-of-flight spectroscopy Physica B+C. 136: 256-259. DOI: 10.1016/S0378-4363(86)80069-9 |
0.341 |
|
1986 |
Trewhella J, Popot JL, Engelman DM, Zaccai G. Neutron diffraction studies of bacteriorhodopsin Physica B+C. 136: 249-251. DOI: 10.1016/S0378-4363(86)80067-5 |
0.535 |
|
1985 |
Dumont ME, Trewhella J, Engelman DM, Richards FM. Stability of transmembrane regions in bacteriorhodopsin studied by progressive proteolysis. The Journal of Membrane Biology. 88: 233-47. PMID 3913776 DOI: 10.1007/Bf01871088 |
0.542 |
|
1985 |
Trewhella J, Appleby CA, Wright PE. N.M.R. studies of high-spin complexes of soybean leghaemoglobin. Interactions between the distal histidine and acetate, formate and fluoride ligands Australian Journal of Chemistry. 39: 317-324. DOI: 10.1071/Ch9860317 |
0.474 |
|
1983 |
Trewhella J, Anderson S, Fox R, Gogol E, Khan S, Engelman D, Zaccai G. Assignment of segments of the bacteriorhodopsin sequence to positions in the structural map Biophysical Journal. 42: 233-241. PMID 6871370 DOI: 10.1016/S0006-3495(83)84391-4 |
0.544 |
|
1982 |
Appleby CA, Trewhella J, Wright PE. Differences in the heme environment of soybean leghemoglobin components shown by 1H-NMR spectroscopy Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 700: 171-177. DOI: 10.1016/0167-4838(82)90094-2 |
0.475 |
|
1980 |
Trewhella J, Wright PE. 1H-NMR studies of ferric soybean leghemoglobin: assignment of hyperfine shifted resonances of complexes with cyanide, nicotinate, pyridine and azide. Biochimica Et Biophysica Acta. 625: 202-20. PMID 7192162 DOI: 10.1016/0005-2795(80)90284-6 |
0.479 |
|
1979 |
Trewhella J, Wright PE. Spin state equilibria in soybean ferric leghemoglobin and its complexes with fomate and acetate. Biochemical and Biophysical Research Communications. 88: 713-21. PMID 572679 DOI: 10.1016/0006-291X(79)92106-5 |
0.455 |
|
1979 |
Trewhella J, Wright PE, Appleby CA. Molecular basis for proton-Dependent anion binding by soybean leghaemoglobin a [28] Nature. 280: 87-88. DOI: 10.1038/280087A0 |
0.521 |
|
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